The incorporation in vitro of labeled amino acids into the proteins of normal and regenerating rat liver

1961 ◽  
Vol 46 (2) ◽  
pp. 335-343 ◽  
Author(s):  
D.J. McCorquodale ◽  
E.G. Veach ◽  
G.C. Mueller
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Regenerating Rat Liver

EVIDENCE FOR THE INDUCTION OF URIDINE AND DEOXY-URIDINE PHOSPHORYLASES OF REGENERATING RAT LIVER IN VITRO

1965 ◽  
Vol 43 (1) ◽  
pp. 41-48 ◽  
Author(s):  
Esther W. Yamada
Keyword(s):  
Amino Acids ◽  
Tissue Culture ◽  
Rat Liver ◽  
Culture Medium ◽  
Specific Activity ◽  
Tissue Culture Medium ◽  
Uridine Phosphorylase ◽  
Regenerating Rat Liver ◽  
Specific Activities

Increases in the specific activities of undine and deoxyuridine phosphorylases of slices of regenerating rat liver were found 4 hours after incubation in tissue-culture medium containing uridine or 6-azauridine. These increases were not found when the tissue-culture medium contained either 8-azaguanine or puromycin, or when it lacked amino acids. Although both uridine and 6-azauridine were more effective in increasing the specific activity of uridine phosphorylase than that of deoxyuridine phosphorylase, azauridine was more effective than uridine in increasing the specific activities of both enzymes.In time studies, in which slices of regenerating rat liver were incubated in tissue-culture medium containing optimal concentrations of uridine, the specific activities of the two enzymes reached maximum levels at 3–4 hours. Puromycin prevented these increases.

scholarly journals STUDY ON THE SITE OF BIOSYNTHESIS OF β-GLUCURONIDASE AND ITS APPEARANCE IN LYSOSOME IN NORMAL AND HYPOXIC RATS

1970 ◽  
Vol 18 (8) ◽  
pp. 529-541 ◽  
Author(s):  
JULIEN L. VAN LANCKER ◽  
PATRICK L. LENTZ
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Liver Enzyme ◽  
Rat Liver ◽  
Microsomal Enzymes ◽  
Enzyme Preparations ◽  
Lysosomal Fraction ◽  
Regenerating Rat Liver ◽  
Cell Fractions

For the purpose of investigating the site of synthesis of β-glucuronidase, the enzyme was purified, after injection of labeled amino acids, from various cell fractions of regenerating rat liver. Enzyme preparations purified from microsomal, lysosomal, mitochondrial, nuclear and supernatant fractions had identical catalytic and electrophoretic properties. In nonhypoxic rats, incorporation was detectable only in the microsomal enzymes and maximum labeling occurred 30 min after the injection of the labeled amino acid. No label was detectable in the enzyme purified from the lysosomal fraction of nonhypoxic animals. Labeling of enzyme purified from lysosomal fraction was, however, significant after 2 hr of hypoxia.

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